ID A0A255EI36_9ACTN Unreviewed; 399 AA.
AC A0A255EI36;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01977};
DE EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_01977};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_01977};
DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01977};
DE Short=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_01977};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01977};
GN Name=pfp {ECO:0000256|HAMAP-Rule:MF_01977};
GN ORFNames=CGZ91_06935 {ECO:0000313|EMBL:OYN91184.1};
OS Parenemella sanctibonifatiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Parenemella.
OX NCBI_TaxID=2016505 {ECO:0000313|EMBL:OYN91184.1, ECO:0000313|Proteomes:UP000216300};
RN [1] {ECO:0000313|EMBL:OYN91184.1, ECO:0000313|Proteomes:UP000216300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 150081 {ECO:0000313|EMBL:OYN91184.1,
RC ECO:0000313|Proteomes:UP000216300};
RA Bernier A.-M., Bernard K., Domingo M.-C.;
RT "Draft whole genome sequences of clinical Proprionibacteriaceae strains.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the
CC first committing step of glycolysis. Uses inorganic phosphate (PPi) as
CC phosphoryl donor instead of ATP like common ATP-dependent
CC phosphofructokinases (ATP-PFKs), which renders the reaction reversible,
CC and can thus function both in glycolysis and gluconeogenesis.
CC Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-
CC PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
CC {ECO:0000256|HAMAP-Rule:MF_01977}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose
CC 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01977};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_01977};
CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000256|HAMAP-Rule:MF_01977}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000256|HAMAP-Rule:MF_01977}.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-Rule:MF_01977}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01977}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Clade 'P' sub-subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01977}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OYN91184.1}.
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DR EMBL; NMVJ01000006; OYN91184.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255EI36; -.
DR OrthoDB; 9802503at2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000216300; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.450; -; 1.
DR HAMAP; MF_01977; Phosphofructokinase_II_P; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR InterPro; IPR011405; PPi-PFK_SMc01852.
DR PANTHER; PTHR45770; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1.
DR PANTHER; PTHR45770:SF11; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF036484; PPi-PFK_SMc01852; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01977};
KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_01977};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01977};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01977};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01977}; Reference proteome {ECO:0000313|Proteomes:UP000216300};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01977}.
FT DOMAIN 4..293
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01977"
FT BINDING 12
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01977"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01977"
FT BINDING 149..151
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01977"
FT BINDING 194..196
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01977"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01977"
FT BINDING 323..326
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01977"
FT SITE 122
FT /note="Important for catalytic activity and substrate
FT specificity; stabilizes the transition state when the
FT phosphoryl donor is PPi; prevents ATP from binding by
FT mimicking the alpha-phosphate group of ATP"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01977"
FT SITE 148
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01977"
SQ SEQUENCE 399 AA; 42823 MW; B689921F75C1053E CRC64;
MAPKVALLTA GGFAPCLSSA VGGLIERYSS VAPEAEIIAY RHGYQGLLSG DYLTVTPQVR
AKAALLHEFG GSPIGNSRVK LTNAADLVKR GLVQEGQDPL QVAAERLQAD GVTILHTIGG
DDTNTTAADL AKYLADHDYG LTVVGLPKTI DNDVVPIKQT LGADTAADMG ARYAQNICSE
HNSGSRMLII HEVMGRNCGW LTAATAQRYR AWLDSREWLP EIGLSREAWD VHAVYVPEAS
IDLKAEAMRL KGIMDEVGNV TIFLSEGAGV ESIVAELEAE GKEVPRDPFG HVKLDKINPG
QWFAEQFAGL LEAEKVMVQK SGYYSRSAAA NDTDLALIAS MTELAVDSAL SGVSGVIGHD
IERDDELRAI EFERIAGGKP FDTRTDWYTA MLADLGQPA
//
